CALL_DROME
ID CALL_DROME Reviewed; 148 AA.
AC P49258; E1JIY2; Q9VBL9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calmodulin-related protein 97A;
DE AltName: Full=Protein androcam;
GN Name=Acam; Synonyms=And, Camr97A; ORFNames=CG17769;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=7980384; DOI=10.1007/bf00554420;
RA Fyrberg C., Parker H., Hutchison B., Fyrberg E.A.;
RT "Drosophila melanogaster genes encoding three troponin-C isoforms and a
RT calmodulin-related protein.";
RL Biochem. Genet. 32:119-135(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: May be involved in calcium-mediated signal transduction.
CC {ECO:0000269|PubMed:7980384}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; X76045; CAA53630.1; -; mRNA.
DR EMBL; AE014297; AAF56511.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95031.1; -; Genomic_DNA.
DR EMBL; AY070783; AAL48405.1; -; mRNA.
DR RefSeq; NP_001163737.1; NM_001170266.1.
DR RefSeq; NP_476988.1; NM_057640.3.
DR PDB; 2LMT; NMR; -; A=1-148.
DR PDB; 2LMU; NMR; -; A=1-148.
DR PDB; 2LMV; NMR; -; A=1-148.
DR PDBsum; 2LMT; -.
DR PDBsum; 2LMU; -.
DR PDBsum; 2LMV; -.
DR AlphaFoldDB; P49258; -.
DR BMRB; P49258; -.
DR SMR; P49258; -.
DR BioGRID; 69379; 27.
DR DIP; DIP-19348N; -.
DR IntAct; P49258; 12.
DR STRING; 7227.FBpp0291175; -.
DR PaxDb; P49258; -.
DR DNASU; 44913; -.
DR EnsemblMetazoa; FBtr0084904; FBpp0084278; FBgn0011273.
DR EnsemblMetazoa; FBtr0301963; FBpp0291175; FBgn0011273.
DR GeneID; 44913; -.
DR KEGG; dme:Dmel_CG17769; -.
DR CTD; 44913; -.
DR FlyBase; FBgn0011273; Acam.
DR VEuPathDB; VectorBase:FBgn0011273; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000162930; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P49258; -.
DR OMA; SEFCAIM; -.
DR PhylomeDB; P49258; -.
DR Reactome; R-DME-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-DME-111933; Calmodulin induced events.
DR Reactome; R-DME-111957; Cam-PDE 1 activation.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DME-163615; PKA activation.
DR Reactome; R-DME-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DME-2025928; Calcineurin activates NFAT.
DR Reactome; R-DME-203615; eNOS activation.
DR Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-DME-8876725; Protein methylation.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR Reactome; R-DME-9619229; Activation of RAC1 downstream of NMDARs.
DR Reactome; R-DME-9648002; RAS processing.
DR BioGRID-ORCS; 44913; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44913; -.
DR PRO; PR:P49258; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011273; Expressed in testis and 7 other tissues.
DR Genevisible; P49258; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0070865; C:investment cone; IDA:FlyBase.
DR GO; GO:0031476; C:myosin VI complex; IPI:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:FlyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0070855; F:myosin VI head/neck binding; IPI:FlyBase.
DR GO; GO:0030048; P:actin filament-based movement; IC:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR039030; Calmodulin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050:SF401; PTHR23050:SF401; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..148
FT /note="Calmodulin-related protein 97A"
FT /id="PRO_0000073546"
FT DOMAIN 7..42
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 43..78
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 80..115
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 116..148
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 105
FT /note="L -> I (in Ref. 1; CAA53630)"
FT /evidence="ECO:0000305"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:2LMT"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:2LMT"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2LMT"
FT TURN 75..81
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2LMT"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:2LMT"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2LMT"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:2LMT"
SQ SEQUENCE 148 AA; 17015 MW; 32DB8DC4B35C6CB8 CRC64;
MSELTEEQIA EFKDAFVQFD KEGTGKIATR ELGTLMRTLG QNPTEAELQD LIAEAENNNN
GQLNFTEFCG IMAKQMRETD TEEEMREAFK IFDRDGDGFI SPAELRFVMI NLGEKVTDEE
IDEMIREADF DGDGMINYEE FVWMISQK
